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dc.contributor.authorBjørlykke, Gry Alettaeng
dc.contributor.authorKvamme, Bjørn Olaveng
dc.contributor.authorSlinde, Erikeng
dc.contributor.authorRaae, Arnt Johaneng
dc.date.accessioned2012-12-06T14:04:49Z
dc.date.available2012-12-06T14:04:49Z
dc.date.issued2012eng
dc.PublishedProtein Expression and Purification 86(2): 151–156eng
dc.identifier.urihttps://hdl.handle.net/1956/6219
dc.description.abstractNeuroglobin (Ngb) exists only in small amounts in salmon brain. In order to study the protein in more detail salmon neuroglobin (sNgb) was cloned, hetereologously expressed in E.coli and purified. The protein had red color and showed the characteristic peaks at 411 nm (metNgb), 415 nm (carboxyNgb) and 424 nm (deoxyNgb). Western analysis showed that sNgb reacted weakly against a rabbit anti human neuroglobin (hNgb) and strongly to a sNgb specific antibody. Our 3Dhomology model of the sNgb indicated modifications adjacent to and in the O2/CO binding site. This may correlate to differences in substrate affinities for the sNgb compared to the hNgb. Also sNgb contained shorter helixes and longer interhelical loops typical for psycrophilic proteins.en_US
dc.language.isoengeng
dc.publisherElsevier Inc.en_US
dc.relation.ispartof<a href="http://hdl.handle.net/1956/6219" target="blank">Sedation and slaughter of Atlantic salmon (Salmo salar, L.) with carbon monoxide, and a possible regulatory role of neuroglobin</a>en_US
dc.subjectNeuroglobineng
dc.subjectAtlantic salmoneng
dc.subjectwestern analysiseng
dc.subjectheme spectrumeng
dc.subjecthomology modeleng
dc.subjectpsycrophiliceng
dc.titleCloning, expression and purification of Atlantic salmon (Salmo salar, L.) neuroglobinen_US
dc.typeJournal article
dc.description.versionsubmittedVersionen_US
dc.rights.holderCopyright 2012 Elsevier Inc. All rights reserved.en_US
dc.identifier.doihttps://doi.org/10.1016/j.pep.2012.09.010
dc.identifier.cristin993100


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